Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ketol-acid reductoisomerase (NADP(+))

Gene

ilvC

Organism
Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.UniRule annotation

Catalytic activityi

(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.UniRule annotation
(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 2 magnesium ions per subunit.UniRule annotation

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (Maeo_0682)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. no protein annotated in this organism
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-valine from pyruvate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (Maeo_0682)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. no protein annotated in this organism
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei47NADPUniRule annotation1
Binding sitei52NADPUniRule annotation1
Active sitei107UniRule annotation1
Binding sitei133NADP; via amide nitrogenUniRule annotation1
Metal bindingi190Magnesium 1UniRule annotation1
Metal bindingi190Magnesium 2UniRule annotation1
Metal bindingi194Magnesium 1UniRule annotation1
Metal bindingi226Magnesium 2UniRule annotation1
Metal bindingi230Magnesium 2UniRule annotation1
Binding sitei251SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi24 – 27NADPUniRule annotation4
Nucleotide bindingi82 – 85NADPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

IsomeraseImported, OxidoreductaseUniRule annotationImported

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation, NADPUniRule annotation, Nucleotide-bindingUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Ketol-acid reductoisomerase (NADP(+))UniRule annotation (EC:1.1.1.86UniRule annotation)
Short name:
KARIUniRule annotation
Alternative name(s):
Acetohydroxy-acid isomeroreductaseUniRule annotation
Alpha-keto-beta-hydroxylacyl reductoisomeraseUniRule annotation
Ketol-acid reductoisomerase type 1UniRule annotation
Ketol-acid reductoisomerase type IUniRule annotation
Gene namesi
Name:ilvCUniRule annotation
Ordered Locus Names:Maeo_1175Imported
OrganismiMethanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)Imported
Taxonomic identifieri419665 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
Proteomesi
  • UP000001106 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi419665.Maeo_1175.

Structurei

3D structure databases

ProteinModelPortaliA6UW80.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 177IlvNInterPro annotationAdd BLAST164
Domaini183 – 324IlvCInterPro annotationAdd BLAST142

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.UniRule annotation
Contains 1 IlvC domain.UniRule annotation
Contains 1 IlvN domain.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04465. Archaea.
COG0059. LUCA.
HOGENOMiHOG000016230.
KOiK00053.
OMAiLDWWKKF.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
HAMAPiMF_00435. IlvC. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
IPR013116. IlvN.
IPR013023. Ketol-acid_reductoisomrdctse.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiPF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.

Sequencei

Sequence statusi: Complete.

A6UW80-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVYYEEDAN YDAVKDKTIA VIGYGSQGMA QSCNMKDSGL NVIVGLRPNG
60 70 80 90 100
ASWEKAKADG HTVMSVEEAA EKADIIHILI PDEVQKDVYN NQIKQHLTEG
110 120 130 140 150
KTLSFSHGYN VHFKYIDPIK GVNVIMVAPK SPGAMVRRTY TEGFGVPGLV
160 170 180 190 200
CVERDETGDA LDIALGMAKA EGLTKAGVIK TTFKEETETD LFGEQAVLCG
210 220 230 240 250
GVTELIKAGF DTLVEAGYSP EMAYFETCNE LKLIVDLIYQ KGLAGMWNDV
260 270 280 290 300
SNTAEYGGFV TRERVINEES RKAMREILKE IQNGKFARDW ALENVSGIPH
310 320
LNAMRRLEDE SLLETTGKKL RKMCGLQKD
Length:329
Mass (Da):36,348
Last modified:August 21, 2007 - v1
Checksum:i8D72B89581B32026
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000743 Genomic DNA. Translation: ABR56752.1.
RefSeqiWP_011973884.1. NC_009635.1.

Genome annotation databases

EnsemblBacteriaiABR56752; ABR56752; Maeo_1175.
GeneIDi5326459.
KEGGimae:Maeo_1175.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000743 Genomic DNA. Translation: ABR56752.1.
RefSeqiWP_011973884.1. NC_009635.1.

3D structure databases

ProteinModelPortaliA6UW80.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi419665.Maeo_1175.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABR56752; ABR56752; Maeo_1175.
GeneIDi5326459.
KEGGimae:Maeo_1175.

Phylogenomic databases

eggNOGiarCOG04465. Archaea.
COG0059. LUCA.
HOGENOMiHOG000016230.
KOiK00053.
OMAiLDWWKKF.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
HAMAPiMF_00435. IlvC. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
IPR013116. IlvN.
IPR013023. Ketol-acid_reductoisomrdctse.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiPF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiA6UW80_META3
AccessioniPrimary (citable) accession number: A6UW80
Entry historyi
Integrated into UniProtKB/TrEMBL: August 21, 2007
Last sequence update: August 21, 2007
Last modified: November 2, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.